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Article

Studies on enzymatic activity and conformational stability of muscle acylphosphatase mutated at conserved lysine residues.

Protein engineering - 1 Jul 1998

Chiti F, Magherini F, Taddei N, Ilardi C, Stefani M, Bucciantini M, Dobson C M, Ramponi G

Abstract excerpt

An oligonucleotide-directed mutagenesis study was carried out on the five acylphosphatase conserved lysine residues to assess their possible participation in enzyme active site formation and their contribution to the enzyme conformational stability. The study was designed to eliminate the ambiguity arising from the presence of a sulfate ion, an enzyme competitive inhibitor, bound to lysine 32 and 68 in the...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 9740373
DOI: 10.1093/protein/11.7.557

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Studies on enzymatic activity and conformational stability of muscle acylphosphatase mutated at conserved lysine residues.PMID 9740373Read ↗

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